ID   A6W7X3_KINRD            Unreviewed;       460 AA.
AC   A6W7X3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABS02912.1};
GN   OrderedLocusNames=Krad_1424 {ECO:0000313|EMBL:ABS02912.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02912.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA   Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000750; ABS02912.1; -; Genomic_DNA.
DR   RefSeq; WP_011981949.1; NC_009664.2.
DR   AlphaFoldDB; A6W7X3; -.
DR   STRING; 266940.Krad_1424; -.
DR   KEGG; kra:Krad_1424; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 3699548at2; -.
DR   Proteomes; UP000001116; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00700; GABAtrnsam; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABS02912.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW   Transferase {ECO:0000313|EMBL:ABS02912.1}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  47169 MW;  BD59C0BC2A336B03 CRC64;
     MTTLSSPDAT SAPAVGGPAL PQEIRLRTEV PGPLSRELAA RRVAAVSAAV GSSMPFYAAV
     AGGGVVVDVD GNSYADLGSG IAVTTVGNAD PAVVAAVGEQ VGRFTHTCFM ITPYDSYVAV
     AERLNALTPG DFPKRTALFS TGAEAVENAV KVARAFTGRQ AVVVFDHAYH GRTNLTMAMT
     AKNMPYKNGF GPFAPEVYRA PLSYPFRDGL DGPTAAARAI ATIEKQVGAA NLAAVVVEPV
     QGEGGFIVPA PGFLPAIAAW ARENGVVFVA DEVQTGIART GAVFASHLEG IEPDLVTIAK
     GVAGGLPLAA VTGRAEILDA PVVGGLGGTY GGNPAACAAA LATLDAVEHE DLPARARQLE
     GVLLRRLHAL AAVDPRVGDV RGRGAMVAVE LVRPGTTEPD AALAKRVAAD AARRGVIVLT
     CGTDGNVLRF LPPLSIPDAL LEEAFDVLDD VFATDRPTAR
//